5oat: Difference between revisions

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-'''Unreleased structure'''
-The entry 5oat is ON HOLD  until Paper Publication
+==PINK1 structure==
+<StructureSection load='5oat' size='340' side='right' caption='[[5oat]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5oat]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OAT FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5oat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oat OCA], [http://pdbe.org/5oat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oat RCSB], [http://www.ebi.ac.uk/pdbsum/5oat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oat ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Mutations in the human kinase PINK1 (hPINK1) are associated with autosomal recessive early-onset Parkinson's disease (PD). hPINK1 activates Parkin E3 ligase activity, involving phosphorylation of ubiquitin and the Parkin ubiquitin-like (Ubl) domain via as yet poorly understood mechanisms. hPINK1 is unusual amongst kinases due to the presence of three loop insertions of unknown function. We report the structure of Tribolium castaneum PINK1 (TcPINK1), revealing several unique extensions to the canonical protein kinase fold. The third insertion, together with autophosphorylation at residue Ser205, contributes to formation of a bowl-shaped binding site for ubiquitin. We also define a novel structural element within the second insertion that is held together by a distal loop that is critical for TcPINK1 activity. The structure of TcPINK1 explains how PD-linked mutations that lie within the kinase domain result in hPINK1 loss-of-function and provides a platform for the exploration of small molecule modulators of hPINK1.
-Authors:
+Structure of PINK1 and mechanisms of Parkinson's disease associated mutations.,Kumar A, Tamjar J, Waddell AD, Woodroof HI, Raimi OG, Shaw AM, Peggie M, Muqit MM, van Aalten DM Elife. 2017 Oct 5;6. pii: e29985. doi: 10.7554/eLife.29985. PMID:28980524<ref>PMID:28980524</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5oat" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aalten, D M.F van]]
+[[Category: Kumar, A]]
+[[Category: Muqit, M M.K]]
+[[Category: Peggie, M]]
+[[Category: Raimi, O G]]
+[[Category: Tamjar, J]]
+[[Category: Waddell, A Y]]
+[[Category: Woodroof, H I]]
+[[Category: Kinase]]
+[[Category: Kinase for phosphorylation]]